Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Calmodulin | required | Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | loss of activity through proteolysis only by ficin digestion | Oryctolagus cuniculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | dependent on | Oryctolagus cuniculus | |
Mg2+ | required | Oryctolagus cuniculus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
16700 | - |
- |
Oryctolagus cuniculus |
44700 | - |
- |
Oryctolagus cuniculus |
125200 | - |
- |
Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Oryctolagus cuniculus | the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme | ? | - |
? | |
additional information | Oryctolagus cuniculus New Zealand White | the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | P18688 AND P12798 | subunits alpha and beta | - |
Oryctolagus cuniculus New Zealand White | P18688 AND P12798 | subunits alpha and beta | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | loss of activity through proteolysis only by ficin digestion | Oryctolagus cuniculus |
phosphoprotein | when PhK is phosphorylated, the alpha subunit is cleaved in the same loop regions (656-748 and 967-1015). A new region (627-662) proximal to the former loop is observed. Additionally, two new regions near the C-terminus of alpha appear, as well as a peptide corresponding to residues 1103-1113 and one of residues 1217-1224. Cys1234 is modified only in the phosphorylated complex. The entire C-terminus from residues 1217 to 1237 may be more exposed in the activated conformer | Oryctolagus cuniculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
psoas | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme | Oryctolagus cuniculus | ? | - |
? | |
additional information | the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme | Oryctolagus cuniculus New Zealand White | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
hexadecamer | (alphabetagammadelta)4 , 4 x 138400, alpha-subunit, + 4 * 125200, beta-subunit, + 4 * 44700, gamma-subunit, + 4 * 16700, delta-subunit, about, mass spectrometry | Oryctolagus cuniculus |
More | mass spectrometric analysis of surface-exposed regions in the hexadecameric phosphorylase kinase complex, overview. Phosphorylase kinase is a 1.3 MDa (alphabetagammadelta)4 enzyme complex, in which alphabetagammadelta protomers associate in D2 symmetry to form two large octameric lobes that are interconnected by four bridges. The alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme. Enzyme structure analysis by mass spectrometry, small-angle X-ray scattering, and transmission electron microscopy | Oryctolagus cuniculus |
Synonyms | Comment | Organism |
---|---|---|
PhK | - |
Oryctolagus cuniculus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Oryctolagus cuniculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.2 | - |
assay at | Oryctolagus cuniculus |